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dc.contributor.authorKoppikar, Anuradha Rajesh
dc.description.abstractO-linked mannose has been implicated in cell-cell and cell-matrix adhesion. Defects in glycosyltransferases that add or extend O-linked mannose on glycoproteins generate neuron migration defects in congenital muscular dystrophies (CMD). The only well characterized O-mannose modified mammalian protein has been the peripheral membrane protein alpha-dystroglycan (±-DG). We propose that there must be other O-mannosylated proteins that modulate the CMD phenotype since O-mannosylation comprises a third of all O-linked glycans in the brain, and a brain ±-DG knockout does not recapitulate all neuronal aspects of CMD. This research proposal aims to develop a chemoenzymatic labeling method to identify those proteins. Elucidating the functional role of O-mannose would contribute towards existing knowledge of how extracellular glycosylation participates in a broad range of human disorders and tissue functions while also paving the way for glycopeptide and enzyme based therapeutics. KEYWORDS: O-Mannose, Neuron Migration, Chemoenzymatic Labeling USING CHEMOENZYMATIC LABELING TO PROBE O-MANNOSE GLYCOSYLATION By ANURADHA R. KOPPIKAR B.S., Georgia Institute of Technology, 2005 A Thesis Submitted to the Graduate Faculty of The University of Georgia in Partial Fulfillment of the Requirements for the Degree MASTER OF SCIENCE ATHENS, GA 2008
dc.subjectneuron migration
dc.subjectchemoenzymatic labeling
dc.titleUsing chemoenzymatic labeling to probe O-mannose glycosylation
dc.description.departmentBiochemistry and Molecular Biology
dc.description.majorBiochemistry and Molecular Biology
dc.description.advisorLance Wells
dc.description.committeeLance Wells
dc.description.committeeMichael Pierce
dc.description.committeeCarl Bergmann
dc.description.committeeMichael Tiemeyer

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